Figure 1.
Figure 1 Structural representations of human blood plasma 2GPI
revealing the extended chain of the five SCR domains. (A) Ribbon
drawing of 2GPI
with consecutive domains labelled I -V. N-linked glycans, as
well as the position of the putative O-linked glycan, Thr130,
are indicated by a ball-and-stick model. -strands
are shown in red and helices in green. (B) Topology diagram of
2GPI.
The central -sheets
of all five domains are labelled B2(-B2")-B3-B4(-B5), the N- and
C-terminal -sheets
are labelled B1'-B2' and B4'-B5', the -helix
and the 3/10 helix are denoted A1 and A2 and numbers of residues
delimiting secondary structure elements are given. Disulfide
bonds are indicated with dashed lines. The positions of
N-glycosylation are given by hexagons; a diamond indicates the
putative O-glycan. Horizontal dashed lines mark domain
boundaries. (C) Ribbon representation of domain III of 2GPI
with labelled secondary structure elements. The two fully
conserved disulfide bonds are shown in yellow. (D) Ribbon
representation of domain V of 2GPI
with labelled secondary structure elements. The three disulfide
bonds are indicated with yellow lines. The aberrant face, which
contains the membrane-binding site, is located on the right-hand
side.
The above figure is reprinted
from an Open Access publication published by Macmillan Publishers Ltd:
EMBO J
(1999,
18,
5166-5174)
copyright 1999.
2GPI
revealing the extended chain of the five SCR domains. (A) Ribbon
drawing of 
-helix
and the 3/10 helix are denoted A1 and A2 and numbers of residues
delimiting secondary structure elements are given. Disulfide
bonds are indicated with dashed lines. The positions of
N-glycosylation are given by hexagons; a diamond indicates the
putative O-glycan. Horizontal dashed lines mark domain
boundaries. (C) Ribbon representation of domain III of